ID   D3HTM8_LEGLN            Unreviewed;       716 AA.
AC   D3HTM8;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE            EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN   OrderedLocusNames=LLO_1893 {ECO:0000313|EMBL:CBJ12274.1};
OS   Legionella longbeachae serogroup 1 (strain NSW150).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=661367 {ECO:0000313|EMBL:CBJ12274.1, ECO:0000313|Proteomes:UP000001060};
RN   [1] {ECO:0000313|EMBL:CBJ12274.1, ECO:0000313|Proteomes:UP000001060}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NSW150 {ECO:0000313|EMBL:CBJ12274.1,
RC   ECO:0000313|Proteomes:UP000001060};
RX   PubMed=20174605; DOI=10.1371/journal.pgen.1000851;
RA   Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D.,
RA   Newton H., Sansom F., Jarraud S., Zidane N., Ma L., Bouchier C.,
RA   Etienne J., Hartland E., Buchrieser C.;
RT   "Analysis of the Legionella longbeachae genome and transcriptome uncovers
RT   unique strategies to cause Legionnaires' disease.";
RL   PLoS Genet. 6:E1000851-E1000851(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC         EC=3.4.21.26; Evidence={ECO:0000256|ARBA:ARBA00001070};
CC   -!- SIMILARITY: Belongs to the peptidase S9A family.
CC       {ECO:0000256|ARBA:ARBA00005228}.
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DR   EMBL; FN650140; CBJ12274.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3HTM8; -.
DR   STRING; 661367.LLO_1893; -.
DR   KEGG; llo:LLO_1893; -.
DR   eggNOG; COG1505; Bacteria.
DR   HOGENOM; CLU_011290_1_1_6; -.
DR   Proteomes; UP000001060; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR023302; Pept_S9A_N.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002470; Peptidase_S9A.
DR   PANTHER; PTHR42881; PROLYL ENDOPEPTIDASE; 1.
DR   PANTHER; PTHR42881:SF2; PROLYL ENDOPEPTIDASE; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   Pfam; PF02897; Peptidase_S9_N; 1.
DR   PRINTS; PR00862; PROLIGOPTASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CBJ12274.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001060};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..716
FT                   /note="prolyl oligopeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003044714"
FT   DOMAIN          34..431
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          492..705
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   716 AA;  80539 MW;  75FDCD148E7A060E CRC64;
     MVGTCCMLKK LMFSLPILVS TSLSVFAQSS FNYPEAKKID QVDGYHGVKV MDPYRWLEDI
     DSNEARSWID AQNQLTNEYL SKITQRDAIK KRLIKLWNYE KYSNPFKAGN HYFYSKNDGL
     QNQNVLYITD SINDPGRVFF DPNKLSNDGT AALVGSSFSN DGRFWAYGIA VSGSDRTEWH
     IRNVETGKDL LDTLEPNRHG GVSWLLDNSG FYYSRFVEVT GKSGQENSVF ENLYFHKLGT
     SQSEDYLVYQ PFPGHFTEAQ VSEDGNWLIL AVSKGSSTHN MIYFKRLDQE KTPIIPLVNN
     LDASYGFIGN DGANFYFQTD KDASKGKVTA INVLAVNPTF RDIIPESRET LLGVSLINNQ
     FIMSYLKDAH SQIKIHDIKG KFIREIALPG IGTVAGFNGK RKDTETFYTY SSYNTPPTIY
     LYNMNTGQSK LFCRAKVDLD PNSYKVEQIF YKSKDGTRIP MFIMHKTSIQ LDGNNPTILY
     GYGGFNIPMI PQFSLSLITW MDMGGVYAVA NLRGGSEYGE SWHQAGMKLN KQNVFDDFIS
     AGEWLIANKY TSNEKLAIFG ASNGGLLVGA VLNQRPDLFG AAVPAVGVMD MLRFGKFTIG
     KAWEVEYGSP DNPEEFRVLY GYSPLHNIKQ DTKYPATLIT TADHDDRVFP AHSFKYAATL
     QDAQSGDAPI LIRIETKAGH GTGKPTDKQI QEVADVYAFL MKNLKINCNQ CFRNRS
//